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HIS Lite™ OG488-Tris NTA Chelator

HIS Lite™ OG488-Tris NTA Chelator is used as a sensitive green fluorescent probe for detecting polyhistidine-labeled proteins in combination with the addition of a heavy metal ion such as Ni2+ in cells, solution and solid surfaces. Fluorescent tris-NTA compounds provide an efficient method for site-specific and stable noncovalent fluorescence labeling of polyhistidine-tagged proteins. In contrast to the transient binding of conventional mono-NTA, the multivalent interaction of tris-NTA conjugated fluorophores form a much more stable complex with polyhistidine-tagged proteins. The high selectivity of tris-NTA compounds toward cumulated histidines enables the selective labeling of proteins in cell lysates and on the surface of live cells. Fluorescent tris-NTA conjugates can be applied for the analysis of a ternary protein complex in solution and on surfaces. AAT Bioquest also offers HIS Lite™ OG488-Tris NTA Complex that can be directly used for the specific and highly sensitive detection of His-tagged fusion proteins without the addition of a heavy metal ion. The transition metal ions (e.g., Ni ion)-mediated complexation of polyhistidine-labeled proteins with fluorescent tris-NTA conjugates provides a sensitive reporter for detecting and monitoring protein-protein interactions in real time.

Spectrum

Product family

NameExcitation (nm)Emission (nm)Extinction coefficient (cm -1 M -1)Quantum yieldCorrection Factor (260 nm)Correction Factor (280 nm)Correction Factor (482 nm)Correction Factor (565 nm)
HIS Lite™ Cy5 Tris NTA Chelator65167025000010.271, 0.420.020.030.0090.09
HIS Lite™ Cy3 Tris NTA Chelator55556915000010.1510.070.073--

References

View all 6 references: Citation Explorer
Heterologous overexpression of active hexokinases from microsporidia Nosema bombycis and Nosema ceranae confirms their ability to phosphorylate host glucose.
Authors: Dolgikh, Viacheslav V and Tsarev, Alexander A and Timofeev, Sergey A and Zhuravlyov, Vladimir S
Journal: Parasitology research (2019): 1511-1518
Systematic analysis of the expression, solubility and purification of a passenger protein in fusion with different tags.
Authors: Bernier, Sarah C and Cantin, Line and Salesse, Christian
Journal: Protein expression and purification (2018): 92-106
Expression, purification, and functional characterisation of flagellin, a TLR5-ligand.
Authors: Hajam, Irshad Ahmed and Dar, Pervaiz Ahmed and Sekar, Shanmugam Chandra and Nanda, Rajakishore and Kishore, Subodh and Bhanuprakash, Veerakyathappa and Ganesh, Kondabattula
Journal: Veterinaria italiana (2013): 181-6
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase.
Authors: Maliekal, Pushpa and Vertommen, Didier and Delpierre, Ghislain and Van Schaftingen, Emile
Journal: Glycobiology (2006): 165-72
Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii.
Authors: Grassick, Alice and Murray, Patrick G and Thompson, Roisin and Collins, Catherine M and Byrnes, Lucy and Birrane, Gabriel and Higgins, Timothy M and Tuohy, Maria G
Journal: European journal of biochemistry (2004): 4495-506
Page updated on November 23, 2024

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Catalog Number12655
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Physical properties

Molecular weight

1443.34

Solvent

DMSO

Spectral properties

Correction Factor (260 nm)

0.31

Correction Factor (280 nm)

0.12

Extinction coefficient (cm -1 M -1)

76000

Excitation (nm)

498

Emission (nm)

526

Storage, safety and handling

H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22

Storage

Freeze (< -15 °C); Minimize light exposure
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Gallery Image 1
Gallery Image 2
His-tagged protein ladder (Lane-1), Non His-tagged BSA (Lane-2), His-tagged Annexin V (Lane-3) and Non His-tagged Protein ladder were separated on a NuPAGE® 4–12% Bis-Tris gel and stained with the HIS Lite™ OG488-Tris NTA-Ni Complex. HIS Lite™ OG488-Tris NTA-Ni Complex shows specificity towards His-tagged protein and                the gel.